ID PERL_MESAU Reviewed; 710 AA. AC Q8R481; DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 10-MAY-2017, entry version 72. DE RecName: Full=Lactoperoxidase {ECO:0000312|EMBL:AAM15535.1}; DE Short=LPO {ECO:0000312|EMBL:AAM15535.1}; DE EC=1.11.1.7 {ECO:0000250|UniProtKB:A5JUY8}; DE AltName: Full=Lacrimal gland peroxidase {ECO:0000312|EMBL:AAM15535.1}; DE Flags: Precursor; GN Name=LPO {ECO:0000312|EMBL:AAM15535.1}; OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036 {ECO:0000312|EMBL:AAM15535.1}; RN [1] {ECO:0000312|EMBL:AAM15535.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lacrimal gland {ECO:0000312|EMBL:AAM15535.1}; RA Paliwal A., Srikantan S., De P.K.; RT "cDNA cloning and regulation of a lactoperoxidase (LPO) from hamster RT lacrimal gland."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000305} RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RC TISSUE=Lacrimal gland {ECO:0000303|PubMed:16469299}; RX PubMed=16469299; DOI=10.1016/j.bbrc.2006.01.095; RA Paliwal A., De P.K.; RT "Marked sexual dimorphism of lacrimal gland peroxidase in hamster: RT repression by androgens and estrogens."; RL Biochem. Biophys. Res. Commun. 341:1286-1293(2006). CC -!- FUNCTION: Antimicrobial agent which utilizes hydrogen peroxide and CC thiocyanate (SCN) to generate the antimicrobial substance CC hypothiocyanous acid (HOSCN). {ECO:0000250|UniProtKB:A5JUY8}. CC -!- CATALYTIC ACTIVITY: 2 phenolic donor + H(2)O(2) = 2 phenoxyl CC radical of the donor + 2 H(2)O. {ECO:0000250|UniProtKB:A5JUY8}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; CC Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE- CC ProRule:PRU00298}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently CC per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16469299}. CC Note=Secreted by the lacrimal gland into tears. CC {ECO:0000269|PubMed:16469299}. CC -!- TISSUE SPECIFICITY: Expressed in the lacrimal gland with higher CC levels and 3-fold higher activity in adult females than males and CC secreted into tears (at protein level). CC {ECO:0000269|PubMed:16469299}. CC -!- INDUCTION: Repressed by the androgen dihydrotestosterone (DHT) and CC the estrogen estradiol (E2) (at protein level). CC {ECO:0000269|PubMed:16469299}. CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF498045; AAM15535.1; -; mRNA. DR RefSeq; NP_001268330.1; NM_001281401.1. DR ProteinModelPortal; Q8R481; -. DR SMR; Q8R481; -. DR PeroxiBase; 4045; MauLPO. DR GeneID; 101830444; -. DR CTD; 4025; -. DR HOVERGEN; HBG000071; -. DR OrthoDB; EOG091G0236; -. DR Proteomes; UP000189706; Genome assembly. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0036393; F:thiocyanate peroxidase activity; IEA:InterPro. DR GO; GO:0042742; P:defense response to bacterium; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 1.10.640.10; -; 1. DR InterPro; IPR010255; Haem_peroxidase. DR InterPro; IPR019791; Haem_peroxidase_animal. DR InterPro; IPR029587; LPO. DR PANTHER; PTHR11475:SF88; PTHR11475:SF88; 1. DR Pfam; PF03098; An_peroxidase; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. PE 1: Evidence at protein level; KW Antimicrobial; Calcium; Complete proteome; Disulfide bond; KW Glycoprotein; Heme; Iron; Metal-binding; Oxidoreductase; Peroxidase; KW Phosphoprotein; Secreted; Signal. FT SIGNAL 1 22 {ECO:0000255}. FT PROPEP 23 98 {ECO:0000250|UniProtKB:P80025}. FT /FTId=PRO_0000433299. FT CHAIN 99 710 Lactoperoxidase. FT {ECO:0000250|UniProtKB:P80025}. FT /FTId=PRO_0000433300. FT ACT_SITE 224 224 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 225 225 Calcium. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 299 299 Calcium. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 301 301 Calcium; via carbonyl oxygen. FT {ECO:0000255|PROSITE-ProRule:PRU00298}. FT METAL 303 303 Calcium. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 305 305 Calcium. {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT METAL 466 466 Iron (heme axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00298}. FT BINDING 223 223 Heme (covalent). {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT BINDING 373 373 Heme (covalent). {ECO:0000255|PROSITE- FT ProRule:PRU00298}. FT SITE 370 370 Transition state stabilizer. FT {ECO:0000255|PROSITE-ProRule:PRU00298}. FT MOD_RES 313 313 Phosphoserine. FT {ECO:0000250|UniProtKB:P80025}. FT CARBOHYD 25 25 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 104 104 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 131 131 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 238 238 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 320 320 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 130 143 {ECO:0000255|PROSITE-ProRule:PRU00298}. FT DISULFID 244 254 {ECO:0000255|PROSITE-ProRule:PRU00298}. FT DISULFID 248 272 {ECO:0000255|PROSITE-ProRule:PRU00298}. FT DISULFID 352 363 {ECO:0000255|PROSITE-ProRule:PRU00298}. FT DISULFID 571 628 {ECO:0000255|PROSITE-ProRule:PRU00298}. FT DISULFID 669 694 {ECO:0000255|PROSITE-ProRule:PRU00298}. SQ SEQUENCE 710 AA; 80219 MW; AD8C9359DB1C270F CRC64; MKVLLRLPAL LASLTLLQMA ASTRNATRTA TIRETVDEVK VQVNKAFLDS RDRLKTDMSN LAPTVRHLSG YLKQAKGRTR TAIRVGQVWE QSLKRLRRMV PLTNVTGQGL DLTSLSWEVG CGHPAPTVTC NISNPYRTIT GDCNNRKNPE LGSANRALAR WLPAEYEDGL SLPFGWTPGK TRNGFPLPQP RDVSNQVLDY LNEEEILDQN RSLLFMQWGQ IVDHDLDFAP ETEMGSDNYS KAQCDELCIQ GDNCFPIMFP KGDPKLKTQG KCLPFFRAGF VCPTSPYQSL AREQINALTS FMDASMVYGS EPSLANRLRN LSSPLGLMAV NEEVSDHGRP LLPFVNVKPS PCEVINRTAG VPCFLAGDSR ASEQILLATS HTLFLREHNR LARELSRLNP QWDGEKLYQE ARRIMGALIQ IITFRDYLPI LLGDELQKWI PPYQGYKETV DPRISNVFTF AFRFGHLEVP STVSRLDENY QPWGSEPELP LHKLFFNTWR VVKDGGIDPL VRGLLAKKAK LAHQDKMMTG ELRNMLFQPN HTVHGFDLAA INIQRCRDHG QPGYNSWRAF CGLSQPKTLE ELSAVLRNEV LAKKLMDLYG TPDNIDIWLG AIAEPLVRRG RVGPLLTCLL GQQFQRIRDG DRFWWENPGV FTEKQRDSLQ KMSFSRLVCD NTGINKVPLN PFQPNSYPHS FVDCSAIEKL DLTPWASVKK //